ArticleJournal of the American Chemical Society2011
Mechanistic insight into the nitrosylation of the [4Fe-4S] cluster of WhiB-like proteins.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
- Advances in BODIPY Derivatives for Antibacterial Phototherapy.Angewandte Chemie (International ed. in English) · 2026Review
- Aromatic patch in whiB-like transcription factors facilitates primary sigma factor interaction in mycobacterium tuberculosis.Communications biology · 2026Article
- Role of hydrogen sulfide in catalyzing the formation of NO-ferroheme.Nitric oxide : biology and chemistry · 2025Article
- Nitrite Causes Nitrosative Stress to Iron Sulfur Clusters.Journal of the American Chemical Society · 2025Article
- WhiB-like proteins: Diversity of structure, function and mechanism.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Val43 residue of NsrR is crucial for the nitric oxide response ofMicrobiology spectrum · 2024Article
- Metalloprotein enabled redox signal transduction in microbes.Current opinion in chemical biology · 2023Review
- Structural basis of dual activation of cell division by the actinobacterial transcription factors WhiA and WhiB.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Elusive Mononitrosylated [FeAngewandte Chemie (International ed. in English) · 2022Article
- Positive (Regulatory) and Negative (Cytotoxic) Effects of Dinitrosyl Iron Complexes on Living Organisms.Biochemistry. Biokhimiia · 2022Review
- Nitric oxide reversibly binds the reduced [2Fe-2S] cluster in mitochondrial outer membrane protein mitoNEET and inhibits its electron transfer activity.Frontiers in molecular biosciences · 2022Article
- Physico-Chemistry of Dinitrosyl Iron Complexes as a Determinant of Their Biological Activity.International journal of molecular sciences · 2021Review
- Structural insights into the functional divergence of WhiB-like proteins in Mycobacterium tuberculosis.Molecular cell · 2021Article
- Nitric Oxide Signaling for Actinorhodin Production in Streptomyces coelicolor A3(2) via the DevS/R Two-Component System.Applied and environmental microbiology · 2021Article
- Sensing mechanisms of iron-sulfur cluster regulatory proteins elucidated using native mass spectrometry.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Interaction of theThe Journal of biological chemistry · 2020Article
- Structural basis of non-canonical transcriptional regulation by the σA-bound iron-sulfur protein WhiB1 in M. tuberculosis.Nucleic acids research · 2020Article
- Light-induced release of nitric oxide from the nitric oxide-bound CDGSH-type [2Fe-2S] clusters in mitochondrial protein Miner2.Nitric oxide : biology and chemistry · 2019Article
- The actinobacterial WhiB-like (Wbl) family of transcription factors.Molecular microbiology · 2018Review
- Nitric Oxide Modulates Endonuclease III Redox Activity by a 800 mV Negative Shift upon [FeJournal of the American Chemical Society · 2018Article
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11 authors.
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Abstract
The reactivity of protein bound iron-sulfur clusters with nitric oxide (NO) is well documented, but little is known about the actual mechanism of cluster nitrosylation. Here, we report studies of members of the Wbl family of [4Fe-4S] containing proteins, which play key roles in regulating developmental processes in actinomycetes, including Streptomyces and Mycobacteria, and have been shown to be NO responsive. Streptomyces coelicolor WhiD and Mycobacterium tuberculosis WhiB1 react extremely rapidly with NO in a multiphasic reaction involving, remarkably, 8 NO molecules per [4Fe-4S] cluster. The reaction is 10(4)-fold faster than that observed with O(2) and is by far the most rapid iron-sulfur cluster nitrosylation reaction reported to date. An overall stoichiometry of [Fe(4)S(4)(Cys)(4)](2-) + 8NO → 2[Fe(I)(2)(NO)(4)(Cys)(2)](0) + S(2-) + 3S(0) has been established by determination of the sulfur products and their oxidation states. Kinetic analysis leads to a four-step mechanism that accounts for the observed NO dependence. DFT calculations suggest the possibility that the nitrosylation product is a novel cluster [Fe(I)(4)(NO)(8)(Cys)(4)](0) derived by dimerization of a pair of Roussin's red ester (RRE) complexes.
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